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G3V801 (NETR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurotrypsin

EC=3.4.21.-
Alternative name(s):
Serine protease 12
Gene names
Name:Prss12
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length761 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations By similarity.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 kringle domain.

Contains 1 peptidase S1 domain.

Contains 3 SRCR domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 761740Neurotrypsin
PRO_0000416843

Regions

Domain85 – 15773Kringle
Domain166 – 267102SRCR 1
Domain273 – 373101SRCR 2
Domain386 – 487102SRCR 3
Domain517 – 760244Peptidase S1
Region505 – 51612Zymogen activation region By similarity

Sites

Active site5621Charge relay system By similarity
Active site6121Charge relay system By similarity
Active site7111Charge relay system By similarity
Site516 – 5172Reactive bond homolog Potential

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation5211N-linked (GlcNAc...) Potential
Glycosylation5691N-linked (GlcNAc...) Potential
Disulfide bond85 ↔ 157 Ref.4
Disulfide bond101 ↔ 141 Ref.4
Disulfide bond130 ↔ 155 Ref.4
Disulfide bond191 ↔ 255 By similarity
Disulfide bond204 ↔ 265 By similarity
Disulfide bond235 ↔ 245 By similarity
Disulfide bond298 ↔ 361 By similarity
Disulfide bond311 ↔ 371 By similarity
Disulfide bond341 ↔ 351 By similarity
Disulfide bond411 ↔ 475 By similarity
Disulfide bond424 ↔ 485 By similarity
Disulfide bond455 ↔ 465 By similarity
Disulfide bond505 ↔ 636 Potential
Disulfide bond547 ↔ 563 By similarity
Disulfide bond651 ↔ 717 By similarity
Disulfide bond680 ↔ 694 By similarity
Disulfide bond707 ↔ 736 By similarity

Experimental info

Sequence conflict1341G → D in CAC35028. Ref.1
Sequence conflict4041S → N in CAC35028. Ref.1
Sequence conflict5151K → T in CAC35028. Ref.1
Sequence conflict5651K → T in CAC35028. Ref.1
Sequence conflict5881E → G in CAC35028. Ref.1
Sequence conflict5921E → D in CAC35028. Ref.1

Secondary structure

................. 761
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
G3V801 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: 215EE73A3CE468EA

FASTA76184,220
        10         20         30         40         50         60 
MALARCVLAV ILGVLSEVAR ADPVLHSPLH RPHPSPPRSQ HAHYLPSSRR PPRTPRFPLP 

        70         80         90        100        110        120 
PRAPAAQRPQ LLSTRHTPPT ISRRCGAGEP WGNATNLGVP CLHWDEVPPF LERSPPASWA 

       130        140        150        160        170        180 
ELRGQPHNFC RSPGGAGRPW CFYRNAQGKV DWGYCDCGQG PALPVIRLVG GKSGHEGRVE 

       190        200        210        220        230        240 
LYHAGQWGTI CDDQWDDADA EVICRQLGLS GIAKAWHQAH FGEGSGPILL DEVRCTGNEL 

       250        260        270        280        290        300 
SIEQCPKSSW GEHNCGHKED AGVSCAPLTD GVIRLSGGKS VHEGRLEVYY RGQWGTVCDD 

       310        320        330        340        350        360 
GWTEMNTYVA CRLLGFKYGK QSSVNHFEGS SRPIWLDDVS CSGKEASFIQ CSRRQWGRHD 

       370        380        390        400        410        420 
CSHREDVGLT CYPDSDGHRL SPGFPIRLMD GENKREGRVE VFVSGQWGTI CDDGWTDKHA 

       430        440        450        460        470        480 
AVICRQLGYK GPARARTMAY FGEGKGPIHM DNVKCTGNEK ALADCVKQDI GRHNCRHSED 

       490        500        510        520        530        540 
AGVICDYYEK KTSGHGNKET LSSGCGLRLL HRRQKRIIGG NNSLRGAWPW QASLRLKSTH 

       550        560        570        580        590        600 
GDGRLLCGAT LLSSCWVLTA AHCFKRYGNN SRSYAVRVGD YHTLVPEEFE QEIGVQQIVI 

       610        620        630        640        650        660 
HRNYRPDSSD YDIALVRLQG SGEQCARLST HVLPACLPLW RERPQKTASN CHITGWGDTG 

       670        680        690        700        710        720 
RAYSRTLQQA AVPLLPKRFC KERYKGLFTG RMLCAGNLQE DNRVDSCQGD SGGPLMCEKP 

       730        740        750        760 
DETWVVYGVT SWGYGCGIKD TPGVYTRVPA FVPWIKSVTS L 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the cDNA encoding rat neurotrypsin."
Hintsch G., Sonderegger P.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[4]"NMR solution structure of the neurotrypsin Kringle domain."
Ozhogina O.A., Grishaev A., Bominaar E.L., Patthy L., Trexler M., Llinas M.
Biochemistry 47:12290-12298(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 84-160, PARTIAL PROTEIN SEQUENCE, DISULFIDE BOND, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ311671 mRNA. Translation: CAC35028.2.
CH473952 Genomic DNA. Translation: EDL82129.1.
RefSeqNP_445956.1. NM_053504.1.
UniGeneRn.86653.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K4RNMR-A84-160[»]
2K51NMR-A84-160[»]
ProteinModelPortalG3V801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000021116.

Protein family/group databases

MEROPSS01.237.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000021116; ENSRNOP00000021116; ENSRNOG00000015353.
GeneID85266.
KEGGrno:85266.

Organism-specific databases

CTD8492.
RGD69238. Prss12.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00740000115025.
HOGENOMHOG000113767.
KOK09624.
OMADDGWTDK.
OrthoDBEOG7RNK07.
PhylomeDBG3V801.
TreeFamTF329295.

Family and domain databases

Gene3D2.40.20.10. 1 hit.
3.10.250.10. 3 hits.
InterProIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00051. Kringle. 1 hit.
PF00530. SRCR. 3 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
PR00258. SPERACTRCPTR.
SMARTSM00130. KR. 1 hit.
SM00202. SR. 3 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 3 hits.
SSF57440. SSF57440. 1 hit.
PROSITEPS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS00420. SRCR_1. 3 hits.
PS50287. SRCR_2. 3 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio617408.
PROG3V801.

Entry information

Entry nameNETR_RAT
AccessionPrimary (citable) accession number: G3V801
Secondary accession number(s): Q99JC8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: November 16, 2011
Last modified: April 16, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references